after induction of acid reflux oesophagitis. Expression of COX-2 and enzyme isoform mPGES-1 are markedly increased in oesophagitis and co-localize in epithelial cells of the basal layer, as well as inflammatory and mesenchymal cells in the lamina propria and submucosa

embryonic fibroblasts deficient in cPGES/p23 decrease the expression of the prostaglandin E2 degrading enzyme, 15-hydroxyprostaglandin dehydrogenase, which catalyzes the inactivating conversion of the PGE2 15-OH to a 15-keto group

fibroblasts deficient in cPGES/p23 decrease the expression of the prostaglandin E2 degrading enzyme, 15-hydroxyprostaglandin dehydrogenase, which catalyzes the inactivating conversion of the PGE2 15-OH to a 15-keto group

the electron-sharing network of the Bombyx mori enzyme includes Asn95, Asp96, and Arg98, the residues contribute to catalytic activity. The C-terminal domain contains the binding site for hydrophobic substrate and PGH2, active site and substrate binding site structures, overview

the isozyme mPGES-1 structure reveals three well-defined active site cavities within the membrane-spanning region in each monomer interface of the trimeric structure. An important determinant of the active site cavity is a small cytosolic domain inserted between transmembrane helices I and II. A a 16-A-deep cone-shaped cavity extending from the cytosolic side into the membrane-spanning region might have a potential role in substrate access. Serine 127 plays a role in the catalytic mechanism, active site structure, overview

concordant induction of terminal prostaglandin E2 synthase with cyclooxygenase-2 leads to the preferred production of prostaglandin E2 over thromboxane B2 and prostaglandin D2, by lipopolysaccharide-stimulated macrophages

(5Z,13E)-(15S)-9alpha,11alpha-epidioxy-15-hydroxyprosta-5,13-dienoate, PGH2, mutation R126A/Q creates a glutathione-dependent reductase which is able to convert prostaglandin H2 to prostaglandin F2alpha

concordant induction of terminal prostaglandin E2 synthase with cyclooxygenase-2 leads to the preferred production of prostaglandin E2 over thromboxane B2 and prostaglandin D2, by lipopolysaccharide-stimulated macrophages

heme is bound to the enzyme subunits and alters the enzyme catalytic specificity, overview. Heme is attached to the bound GSH by an iron-sulfur bond, but heme cannot bind to mPGES2 in the absence of GSH, other sulfhydryl compounds, such as DTT and 2-mercaptoethanol, are unable to promote heme binding to isozyme mPGES2. Bound heme is oxidized by H2O2, but it does not dissociate from mPGES2

two different types of prostaglandin E synthase: 1. GSH-dependent enzyme, 2. GSH-independent enzyme. The genitally organs, especially the deferent duct have mainly GSH-dependent prostaglandin E synthase activity. Heart, spleen and uterus have only the GSH-independent activity. In absence of reduced glutathione the enzyme from deferent duct shows only 3% of the activity in presence of reduced glutathione

in normal breast the enzyme is seen in myoepithelial cells and in stromal fibroblasts and vascular smooth muscle, in breast disease, the enzyme is observed in epithelial cells adjacent to cancer, in scattered foci of fibrocystic disease, in ductal carcinoma in situ and in invasive cancers, in addition to myoepithelial cells

peripheral blood monocyte, no basal expression of enzyme, but strong induction of expression by proinflammatory stimulation via LPS. In alternatively activated M2 monocytes-macrophages, interleukins IL-4, IL-13, and to a lesser extent, IL-10 or interferon IFN-gamma inhibit LPS-induced expression of enzyme. Induction of enzyme expression correlates with changes at the protein level and production of prostaglandin E2

constitutive expression of enzyme is associated with increased prostaglandin E2 production and stimulation of growth. Inhibition of enzyme activity and expression block the release of prostaglandin E2 and decrease cellular proliferation. Antiproliferative effects may be overcome by exogenous prostaglandin E2

cells express both microsomal isoforms mPGES-1 and mPGES-2 and cytosolic isoform cPGES; cells express both microsomal isoforms mPGES-1 and mPGES-2 and cytosolic isoform cPGES. Isoform mPGES-1 contributes most to total activity and is induced by interleukin IL-1beta, which in turn reduces the ability of cells to produce prostaglandin I2

prostaglandin E synthases are mostly concentrated in the oviductal epithelial layer and primarily expressed in the ampulla section of the oviduct and to a lesser extent in the isthmus and the isthmic-ampullary junction; prostaglandin E synthases are mostly concentrated in the oviductal epithelial layer and primarily expressed in the ampulla section of the oviduct and to a lesser extent in the isthmus and the isthmic-ampullary junction, the mPGES-1 protein is highly expressed in the contralateral oviduct; prostaglandin E synthases are mostly concentrated in the oviductal epithelial layer and primarily expressed in the ampulla section of the oviduct and to a lesser extent in the isthmus and the isthmic-ampullary junction, the mPGES-2 is mostly expressed in the ipsilateral oviduct

immunolocalized in extravillous trophoblasts and macrophages, in early gestation also in cytotrophoblasts and syncytiotrophoblasts; immunolocalized to the fibroblasts and macrophages in villous stroma, also in apoptotic early gestational syncytiotrophoblasts

protein expression occurs in luminal epithelial and stromal cells around the implanting blastocyst on day 5 of pregnancy, with the progression of implantation to day 6, the protein is mainly expressed in the cells of the primary decidual zone

endometrium, mainly in luminal and glandular epithelium, higher levels of PGES-1 mRNA occur during pregnancy on days 10-11 when compared with days 12-17, intermediate levels of PGES-1 protein are observed on days 10-13, afterwards, PGES-1 mRNA and protein expression decrease, followed by an increase from days 18-19 or 22-23 of pregnancy, highest mRNA and protein levels are reached on days 24-25

endometrium, mainly in luminal and glandular epithelium, higher levels of PGES-1 mRNA occur during pregnancy on days 10-11 when compared with days 12-17, intermediate levels of PGES-1 protein are observed on days 10-13, afterwards, PGES-1 mRNA and protein expression decrease, followed by an increase from days 18-19 or 22-23 of pregnancy, highest mRNA and protein levels are reached on days 24-25